5y2e: Difference between revisions

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'''Unreleased structure'''


The entry 5y2e is ON HOLD
==Crystal structure of the oligomerization domain of NSP4 from the rotavirus strain NCDV==
<StructureSection load='5y2e' size='340' side='right'caption='[[5y2e]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5y2e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovine_rotavirus_strain_NCDV/G6 Bovine rotavirus strain NCDV/G6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y2E FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5y2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y2e OCA], [https://pdbe.org/5y2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y2e RCSB], [https://www.ebi.ac.uk/pdbsum/5y2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y2e ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NSP4_ROTBN NSP4_ROTBN] Involved in virus morphogenesis. Functions as a receptor for the immature double-layered inner capsid particle (ICP) which transiently buds into the lumen of the rough endoplasmic reticulum during viral maturation.  Enterotoxin that causes a phospholipase C-dependent elevation of the intracellular calcium concentration in host intestinal mucosa cells. Increased concentration of intracellular calcium disrupts the cytoskeleton and the tight junctions, raising the paracellular permeability. Potentiates chloride ion secretion through a calcium ion-dependent signaling pathway, inducing age-dependent diarrhea. To perform this enterotoxigenic role in vivo, NSP4 is probably released from infected enterocytes in a soluble form capable of diffusing within the intestinal lumen and interacting with the plasma membrane receptors on neighboring epithelial cells. Possible receptors for NSP4 are alpha-1/beta-1 and alpha-2/beta-1 integrin heterodimers (By similarity).


Authors:  
==See Also==
 
*[[Acetylcholine binding protein 3D structures|Acetylcholine binding protein 3D structures]]
Description:  
__TOC__
[[Category: Unreleased Structures]]
</StructureSection>
[[Category: Bovine rotavirus strain NCDV/G6]]
[[Category: Large Structures]]
[[Category: Kumar S]]
[[Category: Suguna K]]

Latest revision as of 13:21, 27 March 2024

Crystal structure of the oligomerization domain of NSP4 from the rotavirus strain NCDVCrystal structure of the oligomerization domain of NSP4 from the rotavirus strain NCDV

Structural highlights

5y2e is a 4 chain structure with sequence from Bovine rotavirus strain NCDV/G6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NSP4_ROTBN Involved in virus morphogenesis. Functions as a receptor for the immature double-layered inner capsid particle (ICP) which transiently buds into the lumen of the rough endoplasmic reticulum during viral maturation. Enterotoxin that causes a phospholipase C-dependent elevation of the intracellular calcium concentration in host intestinal mucosa cells. Increased concentration of intracellular calcium disrupts the cytoskeleton and the tight junctions, raising the paracellular permeability. Potentiates chloride ion secretion through a calcium ion-dependent signaling pathway, inducing age-dependent diarrhea. To perform this enterotoxigenic role in vivo, NSP4 is probably released from infected enterocytes in a soluble form capable of diffusing within the intestinal lumen and interacting with the plasma membrane receptors on neighboring epithelial cells. Possible receptors for NSP4 are alpha-1/beta-1 and alpha-2/beta-1 integrin heterodimers (By similarity).

See Also

5y2e, resolution 2.70Å

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